Abstract
The redox behavior of a synthetic hemoprotein, the recombinant human serum albumin (rHSA), incorporating a tetraphenylporphinatoiron derivative (FeP) [rHSA-FeP] was first evaluated using a graphite electrode modified with didodecyldimethylammonium bromide as a promoter. Compared to that of the naked FeP, the redox potential of the Fe(III)/Fe(II) couple in rHSA-FeP shifts in the positive direction, indicating that the central ferrous ion of FeP becomes more difficult to be oxidized by incorporation into the albumin structure.
| Original language | English |
|---|---|
| Pages (from-to) | 1194-1195 |
| Number of pages | 2 |
| Journal | Chemistry Letters |
| Issue number | 10 |
| DOIs | |
| State | Published - 2000 |
| Externally published | Yes |